Serine 15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2

Dumaz, Nicolas; Meek, David W.

doi:10.1093/emboj/18.24.7002

Cited by 455Cancer-related Molecular PathwaysHeat shock proteins researchDNA Repair Mechanisms

Serine 15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2

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Dumaz, Nicolas, Meek, David W.·1999·The EMBO Journal

DOI 10.1093/emboj/18.24.7002PMC PMC1171763

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Abstract

The p53 tumour suppressor protein is a labile transcription factor that is activated and stabilized in response to a wide range of cellular stresses, through a mechanism involving disruption of its interaction with MDM2, a negative regulatory partner. Induction of p53 by DNA damage additionally involves a series of phosphorylation and acetylation modifications, some of which are thought to regulate MDM2 binding. Here we report the effects of introducing mutations at several known or putative N-terminal phosphorylation sites on the transactivation function of p53. These studies highlight phosphorylation of Ser15, a key phosphorylation target during the p53 activation process, as being critical for p53-dependent transactivation. Biochemical data indicate that the mechanism by which phosphorylation of Ser15 stimulates p53-dependent transactivation occurs through increased binding to the p300 coactivator protein. The data also indicate that Ser15-dependent regulation of transactivation is independent of any involvement in modulating MDM2 binding, and that Ser15 phosphorylation alone is not sufficient to block the p53-MDM2 interaction.

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Mutation of multiple p53 phosphorylation sites including S15 and S20 did not abrogate p53 stabilization after DNA damage in cell culture.
“Mutation of multiple phosphorylation sites including S15 and S20 did not abrogate p53 stabilization after DNA damage in cell culture (Ashcroft et al, 1999;Blattner et al, 1999;Dumaz and Meek, 1999).”
From ATM activates p53 by regulating MDM2 oligomerization and E3 processivity (2009) · cites this paper as Dumaz and Meek, 1999

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Authors: Dumaz, N., & Meek, D. W.
Affiliations: University of Dundee (GB)
Corresponding author: Meek, David W.
ORCID: Dumaz, Nicolas
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1999-12-15
Volume: 18
Issue: 24
Pages: 7002-7010
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/18.24.7002
PMC: PMC1171763
OpenAlex: W2098935972
Cited by: 455
References: 55
Citations by year: 2026: 6 · 2025: 1 · 2024: 3 · 2023: 1 · 2022: 6 · 2021: 1 · 2020: 5 · 2019: 9 · 2018: 5 · 2017: 6 · 2016: 8 · 2015: 9 · 2014: 18 · 2013: 22 · 2012: 17
FWCI: 12.41
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion)
Funders: Directorate for Biological Sciences
Medical Research Council
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Keywords: p53, transcriptional activation, MDM2, p300 coactivator, p53-MDM2 interaction, DNA damage response, tumour suppressor
MeSH terms: Cell Line, DNA-Binding Proteins, Humans, Nuclear Proteins, Phosphoserine, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Recombinant Proteins, Serine, Transfection, Transcriptional Activation, Tumor Suppressor Protein p53, Mutagenesis, Site-Directed, Protein Serine-Threonine Kinases, Genes, Reporter, Amino Acid Substitution, Proto-Oncogene Proteins c-mdm2, DNA-Activated Protein Kinase

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Serine 15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2

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